The oxoglutarate dehydrogenase complex is involved in myofibril growth and Z-disc assembly in Drosophila

Myofibrils are long intracellular cables specific to muscles, composed mainly of actin and myosin filaments. The actin and myosin filaments are organized into repeated units called sarcomeres, which form the myofibrils. Muscle contraction is achieved by the simultaneous shortening of sarcomeres, whi...

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Bibliographic Details
Main Authors: González Morales Nicanor
Marescal Océane
Szikora Szilárd
Katzemich Anja
Correia-Mesquita Tuana
Bı́ró Péter
Erdélyi Miklós
Mihály József
Schöck Frieder
Format: Article
Published: 2023
Series:JOURNAL OF CELL SCIENCE 136 No. 13
Subjects:
doi:10.1242/jcs.260717

mtmt:34043007
Online Access:http://publicatio.bibl.u-szeged.hu/27870
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Summary:Myofibrils are long intracellular cables specific to muscles, composed mainly of actin and myosin filaments. The actin and myosin filaments are organized into repeated units called sarcomeres, which form the myofibrils. Muscle contraction is achieved by the simultaneous shortening of sarcomeres, which requires all sarcomeres to be the same size. Muscles have a variety of ways to ensure sarcomere homogeneity. We have previously shown that the controlled oligomerization of Zasp proteins sets the diameter of the myofibril. Here, we looked for Zasp-binding proteins at the Z-disc to identify additional proteins coordinating myofibril growth and assembly. We found that the E1 subunit of the oxoglutarate dehydrogenase complex localizes to both the Z-disc and the mitochondria, and is recruited to the Z-disc by Zasp52. The three subunits of the oxoglutarate dehydrogenase complex are required for myofibril formation. Using super-resolution microscopy, we revealed the overall organization of the complex at the Z-disc. Metabolomics identified an amino acid imbalance affecting protein synthesis as a possible cause of myofibril defects, which is supported by OGDH-dependent localization of ribosomes at the Z-disc.
Physical Description:12
ISSN:0021-9533